PARVG_HUMAN
ID PARVG_HUMAN Reviewed; 331 AA.
AC Q9HBI0; B4DDW5; E7EVM6; Q9BQX5; Q9NSG1;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Gamma-parvin;
GN Name=PARVG;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1).
RX PubMed=11171322; DOI=10.1242/jcs.114.3.525;
RA Olski T.M., Noegel A.A., Korenbaum E.;
RT "Parvin, a 42 kDa focal adhesion protein, related to the alpha-actinin
RT superfamily.";
RL J. Cell Sci. 114:525-538(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Fetal brain;
RX PubMed=12529303; DOI=10.1101/gr.695703;
RA Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S.,
RA Bye J.M., Beare D.M., Dunham I.;
RT "Reevaluating human gene annotation: a second-generation analysis of
RT chromosome 22.";
RL Genome Res. 13:27-36(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
RC TISSUE=Spleen, and Urinary bladder;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Lung, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=11722847; DOI=10.1016/s0378-1119(01)00743-0;
RA Korenbaum E., Olski T.M., Noegel A.A.;
RT "Genomic organization and expression profile of the parvin family of focal
RT adhesion proteins in mice and humans.";
RL Gene 279:69-79(2001).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Probably plays a role in the regulation of cell adhesion and
CC cytoskeleton organization. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with integrin-linked protein kinase and actin.
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q9HBI0; Q9H161: ALX4; NbExp=3; IntAct=EBI-3921217, EBI-11317841;
CC Q9HBI0; Q9BQD7: ANTKMT; NbExp=3; IntAct=EBI-3921217, EBI-713602;
CC Q9HBI0; Q6ZTQ4: CDHR3; NbExp=3; IntAct=EBI-3921217, EBI-12143631;
CC Q9HBI0; Q96M91: CFAP53; NbExp=3; IntAct=EBI-3921217, EBI-742422;
CC Q9HBI0; Q8N4W3: CSF3; NbExp=3; IntAct=EBI-3921217, EBI-12843274;
CC Q9HBI0; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-3921217, EBI-742054;
CC Q9HBI0; G5E9A7: DMWD; NbExp=3; IntAct=EBI-3921217, EBI-10976677;
CC Q9HBI0; P24522: GADD45A; NbExp=3; IntAct=EBI-3921217, EBI-448167;
CC Q9HBI0; Q13418: ILK; NbExp=12; IntAct=EBI-3921217, EBI-747644;
CC Q9HBI0; Q96MP8-2: KCTD7; NbExp=3; IntAct=EBI-3921217, EBI-11954971;
CC Q9HBI0; Q5THT1: KLHL32; NbExp=3; IntAct=EBI-3921217, EBI-10247181;
CC Q9HBI0; Q9UBR4-2: LHX3; NbExp=3; IntAct=EBI-3921217, EBI-12039345;
CC Q9HBI0; P50221: MEOX1; NbExp=3; IntAct=EBI-3921217, EBI-2864512;
CC Q9HBI0; P50222: MEOX2; NbExp=3; IntAct=EBI-3921217, EBI-748397;
CC Q9HBI0; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-3921217, EBI-16439278;
CC Q9HBI0; Q9GZM8: NDEL1; NbExp=3; IntAct=EBI-3921217, EBI-928842;
CC Q9HBI0; Q9NR12: PDLIM7; NbExp=3; IntAct=EBI-3921217, EBI-350517;
CC Q9HBI0; P62487: POLR2G; NbExp=3; IntAct=EBI-3921217, EBI-347928;
CC Q9HBI0; P78424: POU6F2; NbExp=3; IntAct=EBI-3921217, EBI-12029004;
CC Q9HBI0; Q04864: REL; NbExp=3; IntAct=EBI-3921217, EBI-307352;
CC Q9HBI0; Q04864-2: REL; NbExp=3; IntAct=EBI-3921217, EBI-10829018;
CC Q9HBI0; Q14140: SERTAD2; NbExp=3; IntAct=EBI-3921217, EBI-2822051;
CC Q9HBI0; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-3921217, EBI-5235340;
CC Q9HBI0; Q08117: TLE5; NbExp=3; IntAct=EBI-3921217, EBI-717810;
CC Q9HBI0; Q08117-2: TLE5; NbExp=5; IntAct=EBI-3921217, EBI-11741437;
CC Q9HBI0; Q92519: TRIB2; NbExp=5; IntAct=EBI-3921217, EBI-947178;
CC Q9HBI0; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-3921217, EBI-2130429;
CC Q9HBI0; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-3921217, EBI-10241197;
CC Q9HBI0; Q8N6Y0: USHBP1; NbExp=6; IntAct=EBI-3921217, EBI-739895;
CC Q9HBI0; Q9BUY5: ZNF426; NbExp=3; IntAct=EBI-3921217, EBI-743265;
CC Q9HBI0; A0A1U9X8X8; NbExp=3; IntAct=EBI-3921217, EBI-17234977;
CC Q9HBI0; PRO_0000449633 [P0DTD1]: rep; Xeno; NbExp=5; IntAct=EBI-3921217, EBI-25492395;
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion. Cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
CC Note=Constituent of focal adhesions. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9HBI0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HBI0-2; Sequence=VSP_004540, VSP_004541;
CC Name=3;
CC IsoId=Q9HBI0-3; Sequence=VSP_012953, VSP_012954;
CC Name=4;
CC IsoId=Q9HBI0-4; Sequence=VSP_045145, VSP_045146, VSP_045147;
CC Name=5;
CC IsoId=Q9HBI0-5; Sequence=VSP_045146, VSP_045147;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in lymphoid organs,
CC including spleen, thymus, lymph node, bone marrow and peripheral blood
CC leukocytes and moderately in the digestive tract, including stomach,
CC duodenum, jejunum, ileum, ileocecum and appendix, as well as in lung
CC and liver. Also expressed in tumors, but at a lower level than in the
CC corresponding normal tissues. {ECO:0000269|PubMed:11722847}.
CC -!- SIMILARITY: Belongs to the parvin family. {ECO:0000305}.
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DR EMBL; AF237772; AAG27174.1; -; mRNA.
DR EMBL; AL590887; CAC37414.1; -; mRNA.
DR EMBL; AL355092; CAB90188.1; -; mRNA.
DR EMBL; CR456480; CAG30366.1; -; mRNA.
DR EMBL; AK293360; BAG56876.1; -; mRNA.
DR EMBL; AK307294; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL031595; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034406; AAH34406.1; -; mRNA.
DR CCDS; CCDS14057.1; -. [Q9HBI0-1]
DR RefSeq; NP_001131077.1; NM_001137605.2. [Q9HBI0-1]
DR RefSeq; NP_071424.1; NM_022141.6. [Q9HBI0-1]
DR RefSeq; XP_005261759.1; XM_005261702.3. [Q9HBI0-1]
DR AlphaFoldDB; Q9HBI0; -.
DR SMR; Q9HBI0; -.
DR BioGRID; 122059; 48.
DR IntAct; Q9HBI0; 45.
DR MINT; Q9HBI0; -.
DR STRING; 9606.ENSP00000391583; -.
DR ChEMBL; CHEMBL5793; -.
DR iPTMnet; Q9HBI0; -.
DR PhosphoSitePlus; Q9HBI0; -.
DR BioMuta; PARVG; -.
DR DMDM; 20143882; -.
DR EPD; Q9HBI0; -.
DR jPOST; Q9HBI0; -.
DR MassIVE; Q9HBI0; -.
DR MaxQB; Q9HBI0; -.
DR PaxDb; Q9HBI0; -.
DR PeptideAtlas; Q9HBI0; -.
DR PRIDE; Q9HBI0; -.
DR ProteomicsDB; 18673; -.
DR ProteomicsDB; 3899; -.
DR ProteomicsDB; 81556; -. [Q9HBI0-1]
DR ProteomicsDB; 81557; -. [Q9HBI0-2]
DR ProteomicsDB; 81558; -. [Q9HBI0-3]
DR TopDownProteomics; Q9HBI0-2; -. [Q9HBI0-2]
DR Antibodypedia; 27676; 103 antibodies from 25 providers.
DR DNASU; 64098; -.
DR Ensembl; ENST00000356909.7; ENSP00000349378.3; ENSG00000138964.17. [Q9HBI0-3]
DR Ensembl; ENST00000415224.5; ENSP00000416761.2; ENSG00000138964.17. [Q9HBI0-3]
DR Ensembl; ENST00000422871.5; ENSP00000391453.1; ENSG00000138964.17. [Q9HBI0-1]
DR Ensembl; ENST00000444313.8; ENSP00000391583.2; ENSG00000138964.17. [Q9HBI0-1]
DR GeneID; 64098; -.
DR KEGG; hsa:64098; -.
DR MANE-Select; ENST00000444313.8; ENSP00000391583.2; NM_022141.7; NP_071424.1.
DR UCSC; uc003bep.4; human. [Q9HBI0-1]
DR CTD; 64098; -.
DR DisGeNET; 64098; -.
DR GeneCards; PARVG; -.
DR HGNC; HGNC:14654; PARVG.
DR HPA; ENSG00000138964; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 608122; gene.
DR neXtProt; NX_Q9HBI0; -.
DR OpenTargets; ENSG00000138964; -.
DR PharmGKB; PA32952; -.
DR VEuPathDB; HostDB:ENSG00000138964; -.
DR eggNOG; KOG3631; Eukaryota.
DR GeneTree; ENSGT00950000183194; -.
DR HOGENOM; CLU_047624_0_0_1; -.
DR InParanoid; Q9HBI0; -.
DR OMA; FFIPLCD; -.
DR OrthoDB; 871306at2759; -.
DR PhylomeDB; Q9HBI0; -.
DR TreeFam; TF314025; -.
DR PathwayCommons; Q9HBI0; -.
DR SignaLink; Q9HBI0; -.
DR BioGRID-ORCS; 64098; 10 hits in 1069 CRISPR screens.
DR GeneWiki; PARVG; -.
DR GenomeRNAi; 64098; -.
DR Pharos; Q9HBI0; Tbio.
DR PRO; PR:Q9HBI0; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9HBI0; protein.
DR Bgee; ENSG00000138964; Expressed in granulocyte and 144 other tissues.
DR ExpressionAtlas; Q9HBI0; baseline and differential.
DR Genevisible; Q9HBI0; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; TAS:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IBA:GO_Central.
DR GO; GO:0030031; P:cell projection assembly; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; TAS:UniProtKB.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IBA:GO_Central.
DR Gene3D; 1.10.418.10; -; 2.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR028433; Parvin.
DR PANTHER; PTHR12114; PTHR12114; 1.
DR Pfam; PF00307; CH; 2.
DR PIRSF; PIRSF039131; Parvin; 1.
DR SMART; SM00033; CH; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS50021; CH; 2.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative splicing; Cell adhesion;
KW Cell junction; Cell membrane; Cytoplasm; Cytoskeleton; Membrane;
KW Reference proteome; Repeat.
FT CHAIN 1..331
FT /note="Gamma-parvin"
FT /id="PRO_0000121585"
FT DOMAIN 44..151
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 210..317
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 17..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:25944712"
FT VAR_SEQ 1
FT /note="M -> MVPAKEQVPGRCDSTQRCFPGPSNWTGAGGRAGSQPFVGDGTLGTPN
FT FCWDHKEKRAAESQLQAWEAM (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045145"
FT VAR_SEQ 49..70
FT /note="VLMEWINATLLPEHIVVRSLEE -> HTWPSPVTGTGDTICGLARKTW (in
FT isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045146"
FT VAR_SEQ 71..331
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045147"
FT VAR_SEQ 187
FT /note="S -> R (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12529303"
FT /id="VSP_012953"
FT VAR_SEQ 188..331
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12529303"
FT /id="VSP_012954"
FT VAR_SEQ 272..273
FT /note="LH -> IS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12529303"
FT /id="VSP_004540"
FT VAR_SEQ 274..331
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12529303"
FT /id="VSP_004541"
FT CONFLICT Q9HBI0-5:63
FT /note="C -> R (in Ref. 4; AK307294)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 331 AA; 37485 MW; 392BFCDD0B7D86A4 CRC64;
MEPEFLYDLL QLPKGVEPPA EEELSKGGKK KYLPPTSRKD PKFEELQKVL MEWINATLLP
EHIVVRSLEE DMFDGLILHH LFQRLAALKL EAEDIALTAT SQKHKLTVVL EAVNRSLQLE
EWQAKWSVES IFNKDLLSTL HLLVALAKRF QPDLSLPTNV QVEVITIEST KSGLKSEKLV
EQLTEYSTDK DEPPKDVFDE LFKLAPEKVN AVKEAIVNFV NQKLDRLGLS VQNLDTQFAD
GVILLLLIGQ LEGFFLHLKE FYLTPNSPAE MLHNVTLALE LLKDEGLLSC PVSPEDIVNK
DAKSTLRVLY GLFCKHTQKA HRDRTPHGAP N
